PDBsum entry 1glg

Galactose-binding protein

PDB id

1glg

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Contents

			Protein chain

					309 a.a. *

			Ligands

					GAL

			Metals

					_CA

			Waters ×215

* Residue conservation analysis

PDB id:

1glg

Links

Name:

Galactose-binding protein

Title:

Crystallographic analysis of the epimeric and anomeric specificity of the periplasmic transport(slash)chemotactic protein receptor for d- glucose and d-galactose

Structure:

Galactose/glucose-binding protein. Chain: a. Engineered: yes

Source:

Escherichia coli. Organism_taxid: 562

Resolution:

2.00Å

R-factor:

0.167

Authors:

M.N.Vyas,N.K.Vyas,F.A.Quiocho

Key ref:

M.N.Vyas et al. (1994). Crystallographic analysis of the epimeric and anomeric specificity of the periplasmic transport/chemosensory protein receptor for D-glucose and D-galactose. Biochemistry, 33, 4762-4768. PubMed id: 8161535 DOI: 10.1021/bi00182a003

Date:

27-Dec-93

Release date:

31-May-94

PROCHECK

	Headers

	References

Protein chain

P0AEE5 (DGAL_ECOLI) - D-galactose/methyl-galactoside binding periplasmic protein MglB from Escherichia coli (strain K12)

Seq: Struc:					332 a.a. 309 a.a.

Key:

PfamA domain

Secondary structure

CATH domain



		Enzyme reactions

Enzyme class:

E.C.?

[IntEnz] [ExPASy] [KEGG] [BRENDA]

DOI no: 10.1021/bi00182a003	Biochemistry 33:4762-4768 (1994)
PubMed id: 8161535

Crystallographic analysis of the epimeric and anomeric specificity of the periplasmic transport/chemosensory protein receptor for D-glucose and D-galactose.
M.N.Vyas, N.K.Vyas, F.A.Quiocho.

ABSTRACT

The D-glucose/D-galactose-binding protein (M(r) = 33,000) found in the periplasm of bacterial cells serves as the primary high-affinity receptor of active transport for and chemotaxis toward both sugar epimers. This protein from Escherichia coli binds D-glucose with a Kd of 2 x 10(-7) M, which is about 2 times tighter than D-galactose. The 2.0-A resolution crystal structure of the binding protein complexed with D-galactose has been refined to a crystallographic R-factor of 0.167. This structure, combined with that previously refined for the complex with D-glucose [Vyas, N.K., Vyas., M. N., & Quiocho, F. A. (1988) Science 242, 1290-1295], provides understanding, in atomic detail, of recognition of sugar epimers and anomers. In the two complex structures, the sugar ring is positioned identically in the binding site, and each hydroxyl group common to both is involved in very similar cooperative hydrogen-bonding interactions with protein residues and ordered water molecules. Only the beta-anomer of both monosaccharides is bound, with Asp154 OD1 primarily responsible for accepting a hydrogen bond from the anomeric hydroxyl. Recognition of both sugar epimers is accomplished principally by hydrogen bonding of Asp14 OD1 with the equatorial OH4 of D-glucose and OD2 with the axial OH4 of D-galactose. These results are reconciled with equilibrium and fast kinetics data, which indicate binding of both anomers of the two sugars, and further compared with sugar recognition by other periplasmic sugar-binding proteins with specificities for arabinose/galactose/fucose, maltooligosaccharides, and ribose.

Literature references that cite this PDB file's key reference

PubMed id

Reference

21333521

S.Jin, J.V.Veetil, J.R.Garrett, and K.Ye (2011).
Construction of a panel of glucose indicator proteins for continuous glucose monitoring.

Biosens Bioelectron, 26, 3427-3431.

19292879

S.Sooriyaarachchi, W.Ubhayasekera, W.Boos, and S.L.Mowbray (2009).
X-ray structure of glucose/galactose receptor from Salmonella typhimurium in complex with the physiological ligand, (2R)-glyceryl-beta-D-galactopyranoside.

FEBS J, 276, 2116-2124.

PDB code:

3ga5

19194917

J.R.Garrett, X.Wu, S.Jin, and K.Ye (2008).
pH-insensitive glucose indicators.

Biotechnol Prog, 24, 1085-1089.

17473016

M.J.Borrok, L.L.Kiessling, and K.T.Forest (2007).
Conformational changes of glucose/galactose-binding protein illuminated by open, unliganded, and ultra-high-resolution ligand-bound structures.

Protein Sci, 16, 1032-1041.

PDB codes:

2fvy 2fw0

17905834

T.J.Amiss, D.B.Sherman, C.M.Nycz, S.A.Andaluz, and J.B.Pitner (2007).
Engineering and rapid selection of a low-affinity glucose/galactose-binding protein for a glucose biosensor.

Protein Sci, 16, 2350-2359.

17766373

Y.Tian, M.J.Cuneo, A.Changela, B.Höcker, L.S.Beese, and H.W.Hellinga (2007).
Structure-based design of robust glucose biosensors using a Thermotoga maritima periplasmic glucose-binding protein.

Protein Sci, 16, 2240-2250.

PDB code:

2h3h

14709382

H.V.Hsieh, Z.A.Pfeiffer, T.J.Amiss, D.B.Sherman, and J.B.Pitner (2004).
Direct detection of glucose by surface plasmon resonance with bacterial glucose/galactose-binding protein.

Biosens Bioelectron, 19, 653-660.

12736688

L.L.Looger, M.A.Dwyer, J.J.Smith, and H.W.Hellinga (2003).
Computational design of receptor and sensor proteins with novel functions.

Nature, 423, 185-190.

12649277

M.Fehr, S.Lalonde, I.Lager, M.W.Wolff, and W.B.Frommer (2003).
In vivo imaging of the dynamics of glucose uptake in the cytosol of COS-7 cells by fluorescent nanosensors.

J Biol Chem, 278, 19127-19133.

12381848

R.M.de Lorimier, J.J.Smith, M.A.Dwyer, L.L.Looger, K.M.Sali, C.D.Paavola, S.S.Rizk, S.Sadigov, D.W.Conrad, L.Loew, and H.W.Hellinga (2002).
Construction of a fluorescent biosensor family.

Protein Sci, 11, 2655-2675.

12402363

S.Chatterjee, K.Ghosh, A.Dhar, and S.Roy (2002).
Ligand specificity and ligand-induced conformational change in gal repressor.

Proteins, 49, 554-559.

11170207

D.S.Dwyer (2001).
Model of the 3-D structure of the GLUT3 glucose transporter and molecular dynamics simulation of glucose transport.

Proteins, 42, 531-541.

10880979

G.M.Bradbrook, J.R.Forshaw, and S.Pérez (2000).
Structure/thermodynamics relationships of lectin-saccharide complexes: the Erythrina corallodendron case.

Eur J Biochem, 267, 4545-4555.

10630988

M.Muraki, K.Harata, N.Sugita, and K.I.Sato (2000).
Protein-carbohydrate interactions in human lysozyme probed by combining site-directed mutagenesis and affinity labeling.

Biochemistry, 39, 292-299.

PDB codes:

1d6p 1d6q

9873010

C.E.Liu, P.Q.Liu, A.Wolf, E.Lin, and G.F.Ames (1999).
Both lobes of the soluble receptor of the periplasmic histidine permease, an ABC transporter (traffic ATPase), interact with the membrane-bound complex. Effect of different ligands and consequences for the mechanism of action.

J Biol Chem, 274, 739-747.

10559198

L.M.Veenhoff, and B.Poolman (1999).
Substrate recognition at the cytoplasmic and extracellular binding site of the lactose transport protein of Streptococcus thermophilus.

J Biol Chem, 274, 33244-33250.

10398397

U.D.Palanisamy, A.Hussain, S.Iqbal, K.Sproule, and C.R.Lowe (1999).
Design, synthesis and characterisation of affinity ligands for glycoproteins.

J Mol Recognit, 12, 57-66.

9651355

D.G.Vassylyev, H.Tomitori, K.Kashiwagi, K.Morikawa, and K.Igarashi (1998).
Crystal structure and mutational analysis of the Escherichia coli putrescine receptor. Structural basis for substrate specificity.

J Biol Chem, 273, 17604-17609.

PDB code:

1a99

9786918

M.Kasahara, and M.Maeda (1998).
Contribution to substrate recognition of two aromatic amino acid residues in putative transmembrane segment 10 of the yeast sugar transporters Gal2 and Hxt2.

J Biol Chem, 273, 29106-29112.

9309217

F.A.Quiocho, J.C.Spurlino, and L.E.Rodseth (1997).
Extensive features of tight oligosaccharide binding revealed in high-resolution structures of the maltodextrin transport/chemosensory receptor.

Structure, 5, 997.

PDB codes:

1anf 3mbp 4mbp

9433125

S.Elgavish, and B.Shaanan (1997).
Lectin-carbohydrate interactions: different folds, common recognition principles.

Trends Biochem Sci, 22, 462-467.

9245406

S.H.Sleigh, J.R.Tame, E.J.Dodson, and A.J.Wilkinson (1997).
Peptide binding in OppA, the crystal structures of the periplasmic oligopeptide binding protein in the unliganded form and in complex with lysyllysine.

Biochemistry, 36, 9747-9758.

PDB codes:

1rkm 2rkm

8702898

A.Wolf, K.C.Lee, J.F.Kirsch, and G.F.Ames (1996).
Ligand-dependent conformational plasticity of the periplasmic histidine-binding protein HisJ. Involvement in transport specificity.

J Biol Chem, 271, 21243-21250.

8861200

F.A.Quiocho, and P.S.Ledvina (1996).
Atomic structure and specificity of bacterial periplasmic receptors for active transport and chemotaxis: variation of common themes.

Mol Microbiol, 20, 17-25.

8747465

J.R.Tame, E.J.Dodson, G.Murshudov, C.F.Higgins, and A.J.Wilkinson (1995).
The crystal structures of the oligopeptide-binding protein OppA complexed with tripeptide and tetrapeptide ligands.

Structure, 3, 1395-1406.

PDB codes:

1olc 2olb

The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.